Homologous Superfamily

Phosphoinositide-binding clathrin adaptor, domain 2 (IPR014712)

Short name: Clathrin_AP_dom2

Overlapping entries


Clathrin-mediated endocytosis plays an important role in retrieving synaptic vesicles from the plasma membrane following exocytosis, and requires the action of CALM (clathrin assembly lymphoid myeloid leukemia protein) or its homologue AP180 (adaptor protein 180) [PMID: 11239400, PMID: 11161218]. These proteins act to restrict the size of the clathrin-coated vesicles. The phosphoinositide-binding domain regulates the clathrin assembly activity of these proteins. Phosphoinositides control the timing and localisation of endocytic membrane trafficking by recruiting adaptors and other components of the transport machinery, thereby being part of a coincidence detection system in adaptor-mediated vesicle transport [PMID: 16246100].

The N-terminal phosphoinositide-binding domain of CALM and AP180 consist of nine alpha helices forming a solenoid structure. This is most similar to the ENTH domain of epsin, with the first seven helices of epsin superimposing well on those of CALM. However, in epsin the final alpha8 helix folds back across the others, whereas in CALM and AP180 the final three long helices continue the solenoidal pattern [PMID: 11161218].

This superfamily represents this 3-helical closed bundle structural subdomain found in CALM and AP180. This domain that shares structural similarity with the GAT domain (IPR004152). It is usually found C-terminal to the the ENTH-like domain (IPR011417).

GO terms

Biological Process

GO:0048268 clathrin coat assembly

Molecular Function

GO:0005545 1-phosphatidylinositol binding
GO:0030276 clathrin binding

Cellular Component

GO:0030136 clathrin-coated vesicle

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.